ID A0A0D2RXG8_GOSRA Unreviewed; 635 AA.
AC A0A0D2RXG8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|ARBA:ARBA00026121, ECO:0000256|RuleBase:RU369030};
DE EC=6.2.1.3 {ECO:0000256|ARBA:ARBA00026121, ECO:0000256|RuleBase:RU369030};
GN ORFNames=B456_006G052200 {ECO:0000313|EMBL:KJB34186.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB34186.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB34186.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- FUNCTION: Catalyzes the conversion of long-chain fatty acids to their
CC active form acyl-CoAs for both synthesis of cellular lipids, and
CC degradation via beta-oxidation. {ECO:0000256|RuleBase:RU369030}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000256|RuleBase:RU369030};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000256|ARBA:ARBA00004872, ECO:0000256|RuleBase:RU369030}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU369030}.
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DR EMBL; CM001745; KJB34186.1; -; Genomic_DNA.
DR EMBL; CM001745; KJB34188.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2RXG8; -.
DR EnsemblPlants; KJB34186; KJB34186; B456_006G052200.
DR EnsemblPlants; KJB34188; KJB34188; B456_006G052200.
DR Gramene; KJB34186; KJB34186; B456_006G052200.
DR Gramene; KJB34188; KJB34188; B456_006G052200.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000032304; Chromosome 6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:InterPro.
DR CDD; cd05927; LC-FACS_euk; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR045311; LC-FACS_euk.
DR PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43272:SF3; LONG-CHAIN-FATTY-ACID--COA LIGASE 5; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU369030};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU369030};
KW Ligase {ECO:0000256|RuleBase:RU369030};
KW Lipid metabolism {ECO:0000256|RuleBase:RU369030};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU369030};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..449
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 635 AA; 70702 MW; 9850A8A011A232BA CRC64;
MHQCFIINFI LKYIRWFLHL LIFFLFRLAV DFFGDNNYLG TRIRVDGTVG EYKWMTYREA
ATARTAIGCG LIHHGILKGS CIGLYFINRP EWIIADHACS AYSLISVPLY DTLGPDAVKY
IINHAELKAV FCVPQTLNPL LSILSEIPSV RLIVVVGGME NEVPSLPSST GIQIVTYSRL
LNQGRSYLQP FCQPKPDDIA TICYTSGTTG TPKGVVLTHG NLIANAAGFS LAVKFNPTDV
YISYLPLAHI FERFNQINLA HYGVAVGFYQ GDNMRLMDDL ASLRPTLFCS VPRLYNRIYA
GILNAVKESG TLKERLFNAA YNSKKQAIMN GKSPSPIWDR LVFNKIKARL GGRVRFMASG
ASPLSPDVMD FLKICFGGHI IEGYGMTETS CVISCMDEGD ILSGHVGSPN PACEIKLVDV
PEMNYTSDDQ PYPRGEICVR GPIVFQGYYK DEMQTREVLD EDGWLHTGDI GLWHTGGRLK
IIDRKKNIFK LAQGEYIAPE KIENVYAKCK FIAQCFIYGD SLNSSLVAIV SVDQDALKAW
ASSQGIKYKD LEQLCNDPRA RAAVQAEMDA VGRDAQLRGF EFAKSVTLVL EPFTMENGLL
TPTFKIKRAQ AKAYFAKAIS NMYVELTTSD SSHVK
//
